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酵母 F-ATP 合酶的通道形成及其在线粒体通透性转换中的二聚化作用。

Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition.

机构信息

From the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.

the Vollum Institute, Oregon Health and Sciences University, Portland, Oregon 97239-3098, and.

出版信息

J Biol Chem. 2014 Jun 6;289(23):15980-5. doi: 10.1074/jbc.C114.559633. Epub 2014 May 1.

DOI:10.1074/jbc.C114.559633
PMID:24790105
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4047373/
Abstract

Purified F-ATP synthase dimers of yeast mitochondria display Ca(2+)-dependent channel activity with properties resembling those of the permeability transition pore (PTP) of mammals. After treatment with the Ca(2+) ionophore ETH129, which allows electrophoretic Ca(2+) uptake, isolated yeast mitochondria undergo inner membrane permeabilization due to PTP opening. Yeast mutant strains ΔTIM11 and ΔATP20 (lacking the e and g F-ATP synthase subunits, respectively, which are necessary for dimer formation) display a striking resistance to PTP opening. These results show that the yeast PTP originates from F-ATP synthase and indicate that dimerization is required for pore formation in situ.

摘要

经钙离子载体 ETH129 处理后，该离子载体允许电泳摄取钙离子，导致分离的酵母线粒体由于 PTP 开放而发生内膜通透性增加。酵母突变株 ΔTIM11 和 ΔATP20（分别缺乏 e 和 g F-ATP 合酶亚基，这些亚基对于二聚体形成是必需的）对 PTP 开放表现出显著的抗性。这些结果表明酵母 PTP 源自 F-ATP 合酶，并表明二聚化是形成原位孔所必需的。

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本文引用的文献

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Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae.酵母 F1Fo-ATP 合酶二聚体的结构及其在塑造线粒体嵴中的作用。
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